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Yoichi Yoshida

Bio: Yoichi Yoshida is an academic researcher. The author has contributed to research in topics: Hydrolase & Laurolactam. The author has an hindex of 2, co-authored 2 publications receiving 37 citations.
Topics: Hydrolase, Laurolactam, Rhodococcus, Amino acid

Papers
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Journal ArticleDOI
TL;DR: Several ω-laurolactam degrading microorganisms were isolated from soil samples and the deduced amino acid sequence showed high homology with 6-aminohexanoate-cyclic-dimer hydrolase (EC 3.5.2.12) from Arthrobacter sp.
Abstract: Several ω-laurolactam degrading microorganisms were isolated from soil samples These strains were capable of growing in a medium containing ω-laurolactam as sole source of carbon and nitrogen Among them, five strains (T7, T31, U124, U224, and U238) were identified as Cupriavidus sp T7, Acidovorax sp T31, Cupriavidus sp U124, Rhodococcus sp U224, and Sphingomonas sp U238, respectively The ω-laurolactam hydrolyzing enzyme from Rhodococcus sp U224 was purified to homogeneity, and its enzymatic properties were characterized The enzyme acts on ω-octalactam and ω-laurolactam, but other lactam compounds, amides and amino acid amides, cannot be substrates The enzyme gene was cloned, and the deduced amino acid sequence showed high homology with 6-aminohexanoate-cyclic-dimer hydrolase (EC 35212) from Arthrobacter sp KI72 and Pseudomonas sp NK87 Enzymatic synthesis of 12-aminolauric acid was performed using partially purified ω-laurolactam hydrolase from Rhodococcus sp U224

24 citations

Journal ArticleDOI
TL;DR: Nucleotide and amino acid sequence analysis of the four genes indicated that the primary structures of these ω-laurolactam hydrolases are significantly similar to the 6-aminohexanoate-cyclic-dimer hydrolase (EC 3.5.2.12).
Abstract: The genes encoding omega-laurolactam hydrolases from Cupriavidus sp. T7, Acidovorax sp. T31, Cupriavidus sp. U124, and Sphingomonas sp. U238 were cloned and sequenced. Nucleotide and amino acid sequence analysis of the four genes indicated that the primary structures of these omega-laurolactam hydrolases are significantly similar to the 6-aminohexanoate-cyclic-dimer hydrolase (EC 3.5.2.12). These genes were expressed in Escherichia coli, and the omega-laurolactam hydrolysing activity of the recombinant enzymes was compared with that of 6-aminohexanoate-cyclic-dimer hydrolase from Arthrobacter sp. KI72. The enzyme from Acidovorax sp. T31 was most successfully expressed in E. coli. Cell-free extract of the recombinant strain was used for the synthesis of 12-aminolauric acid from omega-laurolactam by "enzymatic transcrystallization," because crystalline omega-laurolactam added into the enzyme solution was converted to crystalline 12-aminolauric acid (> or =97.3% yield). Under the optimum conditions, 208 g/l of 12-aminolauric acid was produced in 17 h. The resulting pure product was identical to authentic 12-aminolauric acid.

13 citations


Cited by
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Journal ArticleDOI
Roland Wohlgemuth1
TL;DR: The ongoing trends to process improvements, cost reductions and increasing quality, safety, health and environment requirements of industrial chemical transformations have strengthened the translation of global biocatalysis research work into industrial applications.

324 citations

Journal ArticleDOI
TL;DR: This critical review presents an introduction to biocatalysis for synthetic chemists, illustrating the breadth of applications for these powerful and selective catalysts in conducting key reaction steps of the past 5 years.
Abstract: This critical review presents an introduction to biocatalysis for synthetic chemists. Advances in biocatalysis of the past 5 years illustrate the breadth of applications for these powerful and selective catalysts in conducting key reaction steps. Asymmetric synthesis of value-added targets and other reaction types are covered, with an emphasis on pharmaceutical intermediates and bulk chemicals. Resources of interest for the non-initiated are provided, including specialized websites and service providers to facilitate identification of suitable biocatalysts, as well as references to recent volumes and reviews for more detailed biocatalytic procedures. Challenges related to the application of biocatalysts are discussed, including how ‘green’ a biocatalytic reaction may be, and trends in biocatalyst improvement through enzyme engineering are presented (152 references).

268 citations

Journal ArticleDOI
TL;DR: Judicious employment of enzyme discovery and improvement tools has resulted in significant advancements that have leveraged the research from laboratory to market thus impacting economic growth; however, there are further opportunities that have not yet been explored.
Abstract: Developments in biocatalysis have been largely fuelled by consumer demands for new products, industrial attempts to improving existing process and minimizing waste, coupled with governmental measures to regulate consumer safety along with scientific advancements. One of the major hurdles to application of biocatalysis to chemical synthesis is unavailability of the desired enzyme to catalyse the reaction to allow for a viable process development. Even when the desired enzyme is available it often forces the process engineers to alter process parameters due to inadequacies of the enzyme, such as instability, inhibition, low yield or selectivity, etc. Developments in the field of enzyme or reaction engineering have allowed access to means to achieve the ends, such as directed evolution, de novo protein design, use of non‐conventional media, using new substrates for old enzymes, active‐site imprinting, altering temperature, etc. Utilization of enzyme discovery and improvement tools therefore provides a feasible means to overcome this problem. Judicious employment of these tools has resulted in significant advancements that have leveraged the research from laboratory to market thus impacting economic growth; however, there are further opportunities that have not yet been explored. The present review attempts to highlight some of these achievements and potential opportunities.

54 citations

Journal ArticleDOI
TL;DR: The results in the present study suggest that AmpA is a good candidate for the study of the mechanism for amide pesticide hydrolysis, genetic engineering of amide herbicide-resistant crops, and bioremediation of amid pesticide-contaminated environments.
Abstract: The bacterial isolate Paracoccus sp. strain FLN-7 hydrolyzes amide pesticides such as diflubenzuron, propanil, chlorpropham, and dimethoate through amide bond cleavage. A gene, ampA, encoding a novel arylamidase that catalyzes the amide bond cleavage in the amide pesticides was cloned from the strain. ampA contains a 1,395-bp open reading frame that encodes a 465-amino-acid protein. AmpA was expressed in Escherichia coli BL21 and homogenously purified using Ni-nitrilotriacetic acid affinity chromatography. AmpA is a homodimer with an isoelectric point of 5.4. AmpA displays maximum enzymatic activity at 40°C and a pH of between 7.5 and 8.0, and it is very stable at pHs ranging from 5.5 to 10.0 and at temperatures up to 50°C. AmpA efficiently hydrolyzes a variety of secondary amine compounds such as propanil, 4-acetaminophenol, propham, chlorpropham, dimethoate, and omethoate. The most suitable substrate is propanil, with K(m) and k(cat) values of 29.5 μM and 49.2 s(-1), respectively. The benzoylurea insecticides (diflubenzuron and hexaflumuron) are also hydrolyzed but at low efficiencies. No cofactor is needed for the hydrolysis activity. AmpA shares low identities with reported arylamidases (less than 23%), forms a distinct lineage from closely related arylamidases in the phylogenetic tree, and has different biochemical characteristics and catalytic kinetics with related arylamidases. The results in the present study suggest that AmpA is a good candidate for the study of the mechanism for amide pesticide hydrolysis, genetic engineering of amide herbicide-resistant crops, and bioremediation of amide pesticide-contaminated environments.

43 citations

Journal ArticleDOI
TL;DR: In this article, a review summarizes the recent progress made in biocatalytic and fermentative production of medium and long-chain α,ω-bifunctional monomers suitable as building blocks for polyamide and polyester synthesis.

43 citations